ID SCYL1_HUMAN Reviewed; 808 AA. AC Q96KG9; A6NJF1; Q96G50; Q96KG8; Q96KH1; Q9HAW5; Q9HBL3; Q9NR53; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 187. DE RecName: Full=N-terminal kinase-like protein; DE AltName: Full=Coated vesicle-associated kinase of 90 kDa; DE AltName: Full=SCY1-like protein 1; DE AltName: Full=Telomerase regulation-associated protein; DE AltName: Full=Telomerase transcriptional element-interacting factor; DE AltName: Full=Teratoma-associated tyrosine kinase; GN Name=SCYL1; Synonyms=CVAK90, GKLP, NTKL, TAPK, TEIF, TRAP; GN ORFNames=HT019; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBUNIT, AND TISSUE RP SPECIFICITY. RC TISSUE=Testis; RX PubMed=12036289; DOI=10.1006/geno.2002.6774; RA Kato M., Yano K., Morotomi-Yano K., Saito H., Miki Y.; RT "Identification and characterization of the human protein kinase-like gene RT NTKL: mitosis-specific centrosomal localization of an alternatively spliced RT isoform."; RL Genomics 79:760-767(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), DNA-BINDING (ISOFORM 6), AND RP SUBCELLULAR LOCATION (ISOFORM 6). RC TISSUE=Cervix carcinoma; RX PubMed=15504359; DOI=10.1016/j.bbrc.2004.09.201; RA Tang Z., Zhao Y., Mei F., Yang S., Li X., Lv J., Hou L., Zhang B.; RT "Molecular cloning and characterization of a human gene involved in RT transcriptional regulation of hTERT."; RL Biochem. Biophys. Res. Commun. 324:1324-1332(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 310-808 (ISOFORM 4). RC TISSUE=Eye, and Teratocarcinoma; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-283. RX PubMed=10843802; DOI=10.1006/geno.2000.6194; RA van Asseldonk M., Schepens M., de Bruijn D., Janssen B., Merkx G., RA Geurts van Kessel A.; RT "Construction of a 350-kb sequence-ready 11q13 cosmid contig encompassing RT the markers D11S4933 and D11S546: mapping of 11 genes and 3 tumor- RT associated translocation breakpoints."; RL Genomics 66:35-42(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-808 (ISOFORM 5). RC TISSUE=Hypothalamus; RA Xiao H., Song H., Gao G., Ren S., Chen Z., Han Z.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION (ISOFORM 6), AND DNA-BINDING (ISOFORM 6). RX PubMed=15963946; DOI=10.1016/j.bbrc.2005.05.172; RA Zhao Y., Zheng J., Ling Y., Hou L., Zhang B.; RT "Transcriptional upregulation of DNA polymerase beta by TEIF."; RL Biochem. Biophys. Res. Commun. 333:908-916(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP INTERACTION WITH AP2B1. RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262; RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., RA Mills I.G., Benmerah A., McMahon H.T.; RT "Role of the AP2 beta-appendage hub in recruiting partners for clathrin- RT coated vesicle assembly."; RL PLoS Biol. 4:E262-E262(2006). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18556652; DOI=10.1074/jbc.m801869200; RA Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y., RA Presley J.F., McPherson P.S.; RT "Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, RT regulates COPI-mediated retrograde traffic."; RL J. Biol. Chem. 283:22774-22786(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP INVOLVEMENT IN SCAR21, AND FUNCTION. RX PubMed=26581903; DOI=10.1016/j.ajhg.2015.10.011; RA Schmidt W.M., Rutledge S.L., Schuele R., Mayerhofer B., Zuechner S., RA Boltshauser E., Bittner R.E.; RT "Disruptive SCYL1 mutations underlie a syndrome characterized by recurrent RT episodes of liver failure, peripheral neuropathy, cerebellar atrophy, and RT ataxia."; RL Am. J. Hum. Genet. 97:855-861(2015). RN [16] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-479; TYR-495; HIS-663 AND SER-755. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Regulates COPI-mediated retrograde protein traffic at the CC interface between the Golgi apparatus and the endoplasmic reticulum CC (PubMed:18556652). Involved in the maintenance of the Golgi apparatus CC morphology (PubMed:26581903). Has no detectable kinase activity in CC vitro (PubMed:18556652). {ECO:0000269|PubMed:18556652, CC ECO:0000269|PubMed:26581903}. CC -!- FUNCTION: Isoform 6 acts as a transcriptional activator. It binds to CC three different types of GC-rich DNA binding sites (box-A, -B and -C) CC in the beta-polymerase promoter region. It also binds to the TERT CC promoter region. {ECO:0000269|PubMed:18556652}. CC -!- SUBUNIT: Interacts with GORAB. Interacts with COPA, COPB1 and COPB2 (By CC similarity). Homooligomer. Interacts with AP2B1. {ECO:0000250, CC ECO:0000269|PubMed:12036289, ECO:0000269|PubMed:16903783}. CC -!- INTERACTION: CC Q96KG9-4; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-12023020, EBI-16429430; CC Q96KG9-4; O15169: AXIN1; NbExp=3; IntAct=EBI-12023020, EBI-710484; CC Q96KG9-4; P26196: DDX6; NbExp=5; IntAct=EBI-12023020, EBI-351257; CC Q96KG9-4; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-12023020, EBI-726510; CC Q96KG9-4; Q13526: PIN1; NbExp=3; IntAct=EBI-12023020, EBI-714158; CC Q96KG9-4; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-12023020, EBI-742388; CC Q96KG9-4; Q15560: TCEA2; NbExp=3; IntAct=EBI-12023020, EBI-710310; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:18556652}. Endoplasmic CC reticulum-Golgi intermediate compartment {ECO:0000269|PubMed:18556652}. CC Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:18556652}. CC Note=Localized to the Endoplasmic reticulum-Golgi intermediate and cis- CC Golgi in an ARF1-independent manner. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Note=Cytoplasmic CC throughout the cell cycle. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Note=Cytoplasmic CC throughout the cell cycle. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome. Note=Cytoplasmic during CC interphase and centrosomal during mitosis, it localizes to the CC centrosomes in a microtubule-independent manner. CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus CC {ECO:0000269|PubMed:15504359}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q96KG9-1; Sequence=Displayed; CC Name=2; Synonyms=Variant 1; CC IsoId=Q96KG9-2; Sequence=VSP_020504; CC Name=3; Synonyms=Variant 2; CC IsoId=Q96KG9-3; Sequence=VSP_020504, VSP_020506; CC Name=4; CC IsoId=Q96KG9-4; Sequence=VSP_020508; CC Name=5; CC IsoId=Q96KG9-5; Sequence=VSP_020503, VSP_020505; CC Name=6; CC IsoId=Q96KG9-6; Sequence=VSP_020507; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12036289}. CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically CC inactive. CC -!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 21 (SCAR21) CC [MIM:616719]: A form of spinocerebellar ataxia, a clinically and CC genetically heterogeneous group of cerebellar disorders due to CC degeneration of the cerebellum with variable involvement of the CC brainstem and spinal cord. SCAR21 is characterized by cerebellar CC atrophy and ataxia with onset in early childhood. Patients also CC manifest recurrent episodes of liver failure, hepatic fibrosis and a CC peripheral neuropathy. {ECO:0000269|PubMed:26581903}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 3]: Non-canonical splice junctions. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG09726.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAG17902.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB047077; BAB55454.1; -; mRNA. DR EMBL; AB051427; BAB55458.1; -; mRNA. DR EMBL; AB051428; BAB55459.1; -; mRNA. DR EMBL; AF297709; AAG17902.1; ALT_FRAME; mRNA. DR EMBL; AP000769; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74399.1; -; Genomic_DNA. DR EMBL; BC009967; AAH09967.2; -; mRNA. DR EMBL; BC069233; AAH69233.1; -; mRNA. DR EMBL; AF255613; AAF81422.1; -; Genomic_DNA. DR EMBL; AF225424; AAG09726.1; ALT_FRAME; mRNA. DR CCDS; CCDS41672.1; -. [Q96KG9-1] DR CCDS; CCDS44646.1; -. [Q96KG9-2] DR RefSeq; NP_001041683.1; NM_001048218.1. [Q96KG9-2] DR RefSeq; NP_065731.3; NM_020680.3. [Q96KG9-1] DR RefSeq; XP_005274177.1; XM_005274120.3. DR AlphaFoldDB; Q96KG9; -. DR SMR; Q96KG9; -. DR BioGRID; 121512; 180. DR CORUM; Q96KG9; -. DR IntAct; Q96KG9; 75. DR MINT; Q96KG9; -. DR STRING; 9606.ENSP00000270176; -. DR DrugBank; DB05036; Grn163l. DR GlyGen; Q96KG9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96KG9; -. DR PhosphoSitePlus; Q96KG9; -. DR BioMuta; SCYL1; -. DR DMDM; 74762671; -. DR EPD; Q96KG9; -. DR jPOST; Q96KG9; -. DR MassIVE; Q96KG9; -. DR MaxQB; Q96KG9; -. DR PaxDb; 9606-ENSP00000270176; -. DR PeptideAtlas; Q96KG9; -. DR ProteomicsDB; 77069; -. [Q96KG9-1] DR ProteomicsDB; 77070; -. [Q96KG9-2] DR ProteomicsDB; 77071; -. [Q96KG9-3] DR ProteomicsDB; 77072; -. [Q96KG9-4] DR ProteomicsDB; 77073; -. [Q96KG9-5] DR ProteomicsDB; 77074; -. [Q96KG9-6] DR Pumba; Q96KG9; -. DR Antibodypedia; 7388; 186 antibodies from 25 providers. DR DNASU; 57410; -. DR Ensembl; ENST00000270176.10; ENSP00000270176.5; ENSG00000142186.18. [Q96KG9-1] DR Ensembl; ENST00000420247.6; ENSP00000408192.2; ENSG00000142186.18. [Q96KG9-2] DR Ensembl; ENST00000533862.5; ENSP00000437254.1; ENSG00000142186.18. [Q96KG9-6] DR GeneID; 57410; -. DR KEGG; hsa:57410; -. DR MANE-Select; ENST00000270176.10; ENSP00000270176.5; NM_020680.4; NP_065731.3. DR UCSC; uc001oea.2; human. [Q96KG9-1] DR AGR; HGNC:14372; -. DR CTD; 57410; -. DR DisGeNET; 57410; -. DR GeneCards; SCYL1; -. DR HGNC; HGNC:14372; SCYL1. DR HPA; ENSG00000142186; Low tissue specificity. DR MalaCards; SCYL1; -. DR MIM; 607982; gene. DR MIM; 616719; phenotype. DR neXtProt; NX_Q96KG9; -. DR OpenTargets; ENSG00000142186; -. DR Orphanet; 466794; Acute infantile liver failure-cerebellar ataxia-peripheral sensory motor neuropathy syndrome. DR PharmGKB; PA31812; -. DR VEuPathDB; HostDB:ENSG00000142186; -. DR eggNOG; KOG1243; Eukaryota. DR GeneTree; ENSGT00930000151054; -. DR HOGENOM; CLU_010392_0_1_1; -. DR InParanoid; Q96KG9; -. DR OMA; NDTSWAG; -. DR OrthoDB; 1508at2759; -. DR PhylomeDB; Q96KG9; -. DR TreeFam; TF313435; -. DR PathwayCommons; Q96KG9; -. DR SignaLink; Q96KG9; -. DR SIGNOR; Q96KG9; -. DR BioGRID-ORCS; 57410; 181 hits in 1210 CRISPR screens. DR ChiTaRS; SCYL1; human. DR GeneWiki; SCYL1; -. DR GenomeRNAi; 57410; -. DR Pharos; Q96KG9; Tbio. DR PRO; PR:Q96KG9; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q96KG9; Protein. DR Bgee; ENSG00000142186; Expressed in apex of heart and 175 other cell types or tissues. DR ExpressionAtlas; Q96KG9; baseline and differential. DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell. DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB. DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004713; F:protein tyrosine kinase activity; NAS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl. DR GO; GO:0048666; P:neuron development; IEA:Ensembl. DR GO; GO:0008104; P:protein localization; IEA:Ensembl. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl. DR CDD; cd14011; PK_SCY1_like; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR PANTHER; PTHR12984:SF3; N-TERMINAL KINASE-LIKE PROTEIN; 1. DR PANTHER; PTHR12984; SCY1-RELATED S/T PROTEIN KINASE-LIKE; 1. DR Pfam; PF00069; Pkinase; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR Genevisible; Q96KG9; HS. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; KW DNA-binding; ER-Golgi transport; Golgi apparatus; Intellectual disability; KW Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Spinocerebellar ataxia; Transcription; Transcription regulation; Transport. FT CHAIN 1..808 FT /note="N-terminal kinase-like protein" FT /id="PRO_0000249541" FT DOMAIN 14..314 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REPEAT 350..388 FT /note="HEAT 1" FT REPEAT 389..427 FT /note="HEAT 2" FT REPEAT 507..545 FT /note="HEAT 3" FT REGION 540..566 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 587..646 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 658..808 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 793..808 FT /note="Interaction with COPB1" FT /evidence="ECO:0000250" FT COILED 761..797 FT /evidence="ECO:0000255" FT COMPBIAS 587..601 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 603..617 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 625..646 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 658..684 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 691..717 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 757..808 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 754 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231" FT VAR_SEQ 603..626 FT /note="TPEGVPAPAPTPVPATPTTSGHWE -> SRPARRPLGDAGGGQGHSRGQQHC FT (in isoform 5)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_020503" FT VAR_SEQ 606..622 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:12036289" FT /id="VSP_020504" FT VAR_SEQ 627..808 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_020505" FT VAR_SEQ 628..711 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12036289" FT /id="VSP_020506" FT VAR_SEQ 678..808 FT /note="VSNSDHKSSKSPESDWSSWEAEGSWEQGWQEPSSQEPPPDGTRLASEYNWGG FT PESSDKGDPFATLSARPSTQPRPDSWGEDNWEGLETDSRQVKAELARKKREERRREMEA FT KRAERKVAKGPMKLGARKLD -> SPTGAAGKLRAPGNRAGRSQAPRSHLLTVHGWPAS FT ITGVAQSPATRATPSLPCLHVPAPSRGQTLGVRTTGRASRLTVDRSRLSWPGRSARSGG FT GRWRPNAPRGRWPRAP (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15504359" FT /id="VSP_020507" FT VAR_SEQ 750..808 FT /note="PRPDSWGEDNWEGLETDSRQVKAELARKKREERRREMEAKRAERKVAKGPMK FT LGARKLD -> DRSRLSWPGRSARSGGGRWRPNAPRGRWPRAP (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020508" FT VARIANT 479 FT /note="P -> L (in dbSNP:rs55977709)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041364" FT VARIANT 495 FT /note="H -> Y (in a metastatic melanoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041365" FT VARIANT 663 FT /note="Q -> H (in dbSNP:rs56076708)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041366" FT VARIANT 755 FT /note="W -> S (in dbSNP:rs56077405)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041367" FT CONFLICT 168..169 FT /note="GN -> AT (in Ref. 2; AAG17902)" FT /evidence="ECO:0000305" FT CONFLICT 530 FT /note="I -> F (in Ref. 7; AAG09726)" FT /evidence="ECO:0000305" FT CONFLICT 574 FT /note="V -> W (in Ref. 7; AAG09726)" FT /evidence="ECO:0000305" SQ SEQUENCE 808 AA; 89631 MW; E87A2957DDCCE937 CRC64; MWFFARDPVR DFPFELIPEP PEGGLPGPWA LHRGRKKATG SPVSIFVYDV KPGAEEQTQV AKAAFKRFKT LRHPNILAYI DGLETEKCLH VVTEAVTPLG IYLKARVEAG GLKELEISWG LHQIVKALSF LVNDCSLIHN NVCMAAVFVD RAGEWKLGGL DYMYSAQGNG GGPPRKGIPE LEQYDPPELA DSSGRVVREK WSADMWRLGC LIWEVFNGPL PRAAALRNPG KIPKTLVPHY CELVGANPKV RPNPARFLQN CRAPGGFMSN RFVETNLFLE EIQIKEPAEK QKFFQELSKS LDAFPEDFCR HKVLPQLLTA FEFGNAGAVV LTPLFKVGKF LSAEEYQQKI IPVVVKMFSS TDRAMRIRLL QQMEQFIQYL DEPTVNTQIF PHVVHGFLDT NPAIREQTVK SMLLLAPKLN EANLNVELMK HFARLQAKDE QGPIRCNTTV CLGKIGSYLS ASTRHRVLTS AFSRATRDPF APSRVAGVLG FAATHNLYSM NDCAQKILPV LCGLTVDPEK SVRDQAFKAI RSFLSKLESV SEDPTQLEEV EKDVHAASSP GMGGAAASWA GWAVTGVSSL TSKLIRSHPT TAPTETNIPQ RPTPEGVPAP APTPVPATPT TSGHWETQEE DKDTAEDSST ADRWDDEDWG SLEQEAESVL AQQDDWSTGG QVSRASQVSN SDHKSSKSPE SDWSSWEAEG SWEQGWQEPS SQEPPPDGTR LASEYNWGGP ESSDKGDPFA TLSARPSTQP RPDSWGEDNW EGLETDSRQV KAELARKKRE ERRREMEAKR AERKVAKGPM KLGARKLD //